在需氧状态下，豚鼠巨噬细胞的NADPH氧化酶可将泛醌-5还原。

Ubiquinone-5 is reduced by superoxide in the aerobic state by NADPH oxidase of guinea pig macrophages.

作者信息

Nakamura M, Murakami M, Umei T, Minakami S

出版信息

FEBS Lett. 1985 Jul 8;186(2):215-8. doi: 10.1016/0014-5793(85)80711-0.

Abstract

The reduction of ubiquinone-5 (Q1) by the phagocytosis-specific NADPH oxidase of guinea pig macrophages was not inhibited by superoxide dismutase (SOD) at concentrations usually used for O2- assay but was inhibited at about 100-times higher concentrations. Titration of the reaction with SOD and a comparison with that of xanthine oxidase showed that the inhibition was not due to the semiquinone oxidation accelerated by a removal of O2- but due to the accelerated dismutation of O2- which otherwise reduces the quinone. Molecular oxygens are therefore preferential electron acceptors in the NADPH oxidase even in the presence of Q1.

摘要

豚鼠巨噬细胞吞噬特异性NADPH氧化酶对泛醌-5（Q1）的还原作用，在通常用于超氧阴离子（O2-）检测的浓度下，不受超氧化物歧化酶（SOD）抑制，但在约高100倍的浓度下受到抑制。用SOD对反应进行滴定，并与黄嘌呤氧化酶的滴定进行比较，结果表明这种抑制不是由于O2-的去除加速了半醌氧化，而是由于O2-的歧化加速，否则O2-会还原醌。因此，即使存在Q1，分子氧仍是NADPH氧化酶中的优先电子受体。